Isolation and characterization of the gene coding for human cytidine deaminase.

Article Details

Citation

Demontis S, Terao M, Brivio M, Zanotta S, Bruschi M, Garattini E

Isolation and characterization of the gene coding for human cytidine deaminase.

Biochim Biophys Acta. 1998 Dec 22;1443(3):323-33.

PubMed ID
9878810 [ View in PubMed
]
Abstract

The human gene coding for cytidine deaminase (CD), the enzyme which catalyzes the deamination of cytidine and deoxycytidine to uridine and deoxyuridine, was isolated and structurally characterized. CD is a single copy gene with a length of 31 kb and consists of four exons. Exon-intron junctions do not bracket functional domains of the encoded protein as the boundary between exons 2 and 3 interrupts the catalytically important zinc-finger domain, which is well conserved along phylogenesis. 5'-RACE and RNase mapping experiments identify one major and multiple other minor transcription initiation sites, which are present in placenta as well as in the myeloid cell lines, HL-60 and U937. The 5'-flanking region of the gene contains an orientation-dependent functional promoter and is characterized by the presence of several potential sites for the binding of known transcriptional factors.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Cytidine deaminaseP32320Details